› 1cg6

X-ray diffraction
1.7Å resolution

STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH 5'-DEOXY-5'-METHYLTHIOADENOSINE AND SULFATE AT 1.7 A RESOLUTION

Released:
DOI: 10.2210/pdb1cg6/pdb
PDB entry 1cg6 coloured by chain, front view.
PDB entry 1cg6 coloured by chain, side view.
PDB entry 1cg6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis.
Appleby TC, Erion MD, Ealick SE
Structure 7 629-41 (1999)
PMID: 10404592

Function and Biology Details

Reaction catalysed: 
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171545 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-methyl-5'-thioadenosine phosphorylase Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 31.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13126 (Residues: 1-283; Coverage: 100%)
Gene names: MSAP, MTAP
Sequence domains: Phosphorylase superfamily
Structure domains: Nucleoside phosphorylase domain

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand MTA 1 x MTA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P321
Unit cell:
a: 122.83Å b: 122.83Å c: 45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Structural analyses reveal two distinct families of nucleoside phosphorylases.
Pugmire et al. (2002)
3 more

7 mentions without citation

Strained Conformations of Nucleosides in Active Sites of Nucleoside Phosphorylases.
Il'icheva et al. (2020)
6 more